Friend of Prmt1, a Novel Chromatin Target of Protein Arginine Methyltransferases

Dijk, Thamar B. van; Gillemans, Nynke; Stein, Cláudia; Fanis, Pavlos; Demmers, Jeroen; Corput, Mariëtte van de; Essers, Jeroen; Grosveld, Frank; Bauer, Uta‐Maria; Philipsen, Sjaak

doi:10.1128/mcb.00645-09

Cited by 47 publications

(71 citation statements)

References 53 publications

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“…Like the nuclear SMN, the expressed HB-FOP was extracted more efficiently under the high salt condition than the low salt condition ( Figure 3B). This is consistent with the report of van Dijk et al [26] which demonstrated that FOP was associated with chromatin, localized mainly in facultative heterochromatin region, and thus was extracted mostly under high salt conditions. Biotin affinity Figure 3C and Table 1 and Supplementary Table 3).…”

Section: The Fop-associating Smn Complexes Do Not Contain U1 and U2 Ssupporting

confidence: 93%

“…FOP is also required for the association of SMN complexes with a number of hnRNPs and RNA binding proteins (Step 3 in Figure 5). Based on these data and the previous reports [26], we propose that FOP-SMN complex has a role in retaining spliced and/or unspliced mRNAs in near the transcription sites on chromosome. This does not conflict to the previous notion that FOP has a critical role in specific mRNA transcriptional regulation and mRNA export [27,28].…”

Section: Discussionsupporting

confidence: 80%

“…Our results also suggest that the use of HB-FOP as affinity bait isolates preferentially the latter SMN complex(FOP-SMN complex) (Step 2 in Figure 5). In addition, the quantitative analysis of the components of the endogenous nuclear SMN complexes before and after the knockdown of FOP suggests that the FOP-SMN complex is retained on chromatin [26] possibly via the association with histones (Step 3 in Figure 5). FOP is also required for the association of SMN complexes with a number of hnRNPs and RNA binding proteins (Step 3 in Figure 5).…”

Section: Discussionmentioning

confidence: 99%

“…Anti-FLAG-M2, anti-coilin p80, and anti-FLAG-M2-conjugated agarose beads were obtained from Sigma-Aldrich. Antibody to FOP (KT64) was prepared as described [26]. Anti-GAPDH was obtained from Ambion.…”

Section: Reagents and Antibodiesmentioning

confidence: 99%

“…As noted by alternative names of FOP such as SRAG (small protein rich in arginine and glycine) [25] and CHTOP (Chromatin target of Prmt1) [26], human FOP has a central glycine-ariginine-rich (GAR) domain containing 26 RG/GR repeats that is recognized and methylated with Prmt1, localized mainly in the nuclear speckles and tightly associated with facultative chromatin in interphase cells [26]. The C-terminus of FOP also harbors a duplication of the sequence LDXXLDAYM (where "X" is any amino acid) [26]. FOP is expressed widely among tissues and cell lines [25], and is highly conserved in all vertebrates, while no orthologs was identified so far in yeast, worm, and fly.…”

Section: Introductionmentioning

confidence: 99%

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Friend of Prmt1, FOP is a Novel Component of the Nuclear SMN Complex Isolated Using Biotin Affinity Purification

Izumikawa¹,

Ishikawa²,

Yoshikawa³

et al. 2014

J Proteomics Bioinform

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Section: The Fop-associating Smn Complexes Do Not Contain U1 and U2 Ssupporting

confidence: 93%

Section: Discussionsupporting

confidence: 80%

Section: Discussionmentioning

confidence: 99%

Section: Reagents and Antibodiesmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 3 more Smart Citations

Friend of Prmt1, FOP is a Novel Component of the Nuclear SMN Complex Isolated Using Biotin Affinity Purification

Izumikawa¹,

Ishikawa²,

Yoshikawa³

et al. 2014

J Proteomics Bioinform

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Protein arginine methylation of SERBP1 by protein arginine methyltransferase 1 affects cytoplasmic/nuclear distribution

Lee¹,

Hsieh²,

Chen³

et al. 2012

J of Cellular Biochemistry

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Protein arginine methylation regulates a broad array of cellular processes. SERBP1 implicated in tumor progression through its putative involvement in the plaminogen activator protease cascade, is an RNA-binding protein containing an RG-rich domain and an RGG box domain that might be methylated by protein arginine N-methyltransferases (PRMTs). Asymmetric dimethylarginine (aDMA) was detected in SERBP1 and an indirect methyltransferase inhibitor adenosine dialdehyde (AdOx) significantly reduced the methylation signals. Arginines in the middle RG and C-terminal RGG region of SERBP1 are methylated based on the analyses of different deletion constructs. The predominant type I protein arginine methyltransferase PRMT1 co-immunoprecipitated with SERBP1 and the level of bound PRMT1 decreased upon the addition of AdOx. Recombinant PRMT1 methylated SERBP1 and knockdown of PRMT1 significantly reduced the aDMA level of SERBP1, indicating that SERBP1 is specifically methylated by PRMT1. Immunofluorescent analyses of endogenous SERBP1 showed predominant cytoplasmic localization of SERBP1. Treatment of AdOx or PRMT1 siRNA increased the nuclear localization of SERBP1. Analyses of different deletions indicated that the middle RG region is important for the nuclear localization while both N- and C- terminus are required for nuclear export. Low methylation of the C-terminal RGG region also favors nuclear localization. In conclusion, the RG-rich and RGG box of SERBP1 is asymmetrically dimethylated by PRMT1 and the modification affects protein interaction and intracellular localization of the protein. These findings provide the basis for dissecting the roles of SERBP1.

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Epigenetic dysregulation of leukaemic HOX code in MLL‐rearranged leukaemia mouse model

Kong

et al. 2013

The Journal of Pathology

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HOX genes are frequently dysregulated in human leukaemia with the gene rearrangement between mixed lineage leukaemia (MLL) and partner genes. The resultant MLL fusion proteins are known to mediate leukaemia through disruption of the normal epigenetic regulation at the target gene loci. To elucidate the pathogenic role of MLL fusion proteins in HOX dysregulation in leukaemia, we generated a novel haematopoietic lineage-specific Mll-Een knock-in mouse model using a Cre-mediated inversion strategy. The Mll(Een) (/+) invertor mice developed acute myeloid leukaemia, with organomegaly of the spleen, liver and mesenteric lymph nodes caused by infiltration of blast cells. Using Mll-Een-expressing leukaemic cell lines derived from bone marrow of Mll(Een) (/+) mutant mice, we showed that induction of Hox genes in leukaemic cells was associated with hypomethylated promoter regions and an aberrant active chromatin state at the Hox loci. Knock-down of Prmt1 was insufficient to reverse the active chromatin status and the hypomethylated Hox loci, suggesting that Prmt1-mediated histone arginine methylation was only partially involved in the maintenance of Hox expression in leukaemic cells. Furthermore, in vivo analysis of bone marrow cells of Mll(Een) (/+) mice revealed a Hox expression profile similar to that of wild-type haematopoietic stem cells. The leukaemic Hox profile was highly correlated with aberrant hypomethylation of Hox promoters in the mutant mice, which highlights the importance of DNA methylation in leukaemogenic mechanisms induced by MLL fusion proteins. Our results point to the involvement of dynamic epigenetic regulations in the maintenance of the stem cell-like HOX code that initiates leukaemic stem cells in MLL-rearranged leukaemia. This provides insights for the development of alternative strategies for leukaemia treatment.

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Friend of Prmt1, a Novel Chromatin Target of Protein Arginine Methyltransferases

Cited by 47 publications

References 53 publications

Friend of Prmt1, FOP is a Novel Component of the Nuclear SMN Complex Isolated Using Biotin Affinity Purification

Friend of Prmt1, FOP is a Novel Component of the Nuclear SMN Complex Isolated Using Biotin Affinity Purification

Protein arginine methylation of SERBP1 by protein arginine methyltransferase 1 affects cytoplasmic/nuclear distribution

Epigenetic dysregulation of leukaemic HOX code in MLL‐rearranged leukaemia mouse model

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